title: Models of delta-hemolysin membrane channels and crystal structures.
abstract: Molecular modeling and energy calculations have been used to study how delta-hemolysin and melittin helices may aggregate on membrane surfaces and insert through membranes to form channels. In these models adjacent antiparallel amphipathic helices form planar "raft" structures, in which one surface is hydrophobic and the other hydrophilic. Models of delta-hemolysin crystal structure were developed using these "rafts." These models are based on the unit cell constants and the crystal symmetry obtained from the preliminary crystal data. Energy calculations favor channel models of delta-hemolysin with six or eight monomers per channel.
authors.affiliation: Laboratory of Mathematical Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892.
authors.forename: G
authors.initials: G
authors.lastname: Raghunathan
authors.forename: P
authors.initials: P
authors.lastname: Seetharamulu
authors.forename: B R
authors.initials: BR
authors.lastname: Brooks
authors.forename: H R
authors.initials: HR
authors.lastname: Guy
mesh_terms: D000596:Amino Acids / Q000378:metabolism; D002462:Cell Membrane / Q000737:chemistry*; D006460:Hemolysin Proteins / Q000737:chemistry*; D008051:Lipid Bilayers / Q000737:chemistry; D008555:Melitten / Q000737:chemistry; D008958:Models, Molecular; D011487:Protein Conformation; D014961:X-Ray Diffraction
chemical_list: D000596:Amino Acids; D006460:Hemolysin Proteins; D008051:Lipid Bilayers; D008555:Melitten